PDBsum entry 1so9

Metal transport

PDB id: 1so9

Contents

Protein chain

131 a.a. *

* Residue conservation analysis

PDB id:

1so9

Name:

Metal transport

Title:

Solution structure of apocox11, 30 structures

Structure:

CytochromE C oxidase assembly protein ctag. Chain: a. Fragment: c-terminal soluble domain. Engineered: yes

Source:

Sinorhizobium meliloti. Organism_taxid: 382. Gene: ctag, r00908, smc00012. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

30 models

Authors:

L.Banci,I.Bertini,F.Cantini,S.Ciofi-Baffoni,L.Gonnelli,S.Mangani, Structural Proteomics In Europe (Spine)

Key ref:

L.Banci et al. (2004). Solution structure of Cox11, a novel type of beta-immunoglobulin-like fold involved in CuB site formation of cytochrome c oxidase. J Biol Chem, 279, 34833-34839. PubMed id: 15181013 DOI: 10.1074/jbc.M403655200

Date:

13-Mar-04 Release date: 10-Aug-04

Protein chain

Q92RG6  (COXZ_RHIME) -  Cytochrome c oxidase assembly protein CtaG from Rhizobium meliloti (strain 1021)

Seq: 198 a.a.

Struc: 131 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1074/jbc.M403655200

J Biol Chem 279:34833-34839 (2004)

PubMed id: 15181013

Solution structure of Cox11, a novel type of beta-immunoglobulin-like fold involved in CuB site formation of cytochrome c oxidase.

L.Banci, I.Bertini, F.Cantini, S.Ciofi-Baffoni, L.Gonnelli, S.Mangani.

ABSTRACT

Cytochrome c oxidase assembly process involves many accessory proteins including Cox11, which is a copper-binding protein required for Cu incorporation into the Cu(B) site of cytochrome c oxidase. In a genome wide search, a number of Cox11 homologs are found in all of the eukaryotes with complete genomes and in several Gram-negative bacteria. All of them possess a highly homologous soluble domain and contain an N-terminal fragment that anchors the protein to the membrane. An anchor-free construct of 164 amino acids was obtained from Sinorhizobium meliloti, and the first structure of this class of proteins is reported here. The apoform has an immunoglobulin-like fold with a novel type of beta-strand organization. The copper binding motif composed of two highly conserved cysteines is located on one side of the beta-barrel structure. The apoprotein is monomeric in the presence of dithiothreitol, whereas it dimerizes in the absence of the reductant. When copper(I) binds, NMR and extended x-ray absorption fine structure (EXAFS) data indicate a dimeric protein state with two thiolates bridging two copper(I) ions. The present results advance the knowledge on the poorly understood molecular aspects of cytochrome c oxidase assembly.

Selected figure(s)

Figure 1.
FIG. 1. Solution structure of apoCox11 (residues 20-151). The radius of the tube is proportional to the backbone root mean square deviation of each residue. The secondary structure elements are shown ( -strands in gray and helices in black). The two black spheres indicate the sulfur atoms of Cys-100 and Cys-102, whereas the white sphere represents the N of Lys-97.

Figure 3.
FIG. 3. Comparison between the structures and the two-dimensional topology of apoCox11 (A), a linker domain of a bacterial sialidase (Protein Data Bank code 1eut [PDB] ) (B), and a motile major sperm protein of A. suum (Protein Data Bank code 1msp [PDB] ) (C). The side chains of the Cys-100 and Cys-102 are indicated. The dashed lines indicate sheet formation between two -strands. -Strands a, b, c, e, f, and g (colored gray) are common to all of the Ig-like domains.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2004, 279, 34833-34839) copyright 2004.

Figures were selected by the author.